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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 25, Number 9
BKCSDE 25(9)
September 20, 2004 

Effect of Linker for Immobilization of Glutathione on BSA-Assembled Controlled Pore Glass Beads
Li-Hua Chen, Young-Seo Choi, Jung Won Park, Joseph Kwon, Rong-Shun Wang, Taehoon Lee, Sung Ho Ryu, Joon Won Park*
Glutathione (GSH), Glutathione-S-transferase (GST), Controlled pore glass (CPG), Linker, Bovine serum albumin (BSA)
Controlled pore glass bead was modified with bovine serum albumin (BSA), and glutathione (GSH) was immobilized through three kinds of linkers on top of BSA. Bis(3-sulfo-N-hydroxysuccinimide suberate) sodium salt (BS3), N-hydroxysuccinimide 3-(2-pyridyldithio)propionate (SPDP), or N-hydroxysuccinimide 4-maleimidobutyrate (GMBS) was introduced into the BSA-bound matrix. Subsequently, GSH was immobilized by addition of thiol side chain into the maleimido moiety, replacing a disulfide group, or formation of an amide group upon releasing 3-sulfo-N-hydroxysuccimide group. It was observed that conjugation methodology played a critical role for activity of the immobilized GSH. SDS-PAGE chromatogram showed that the matrix of glutathione immobilized on BSA through GMBS manifested high selectivity towards glutathione-Stransferase (GST) in cell lysate.
1366 - 1370
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